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. 2019 Apr 15;10:1747. doi: 10.1038/s41467-019-09743-4

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Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — Quantifying long-range scalar ¹³C–¹³C couplings. a Two examples of strips used to quantify long-range ¹³C^δ–¹³C^α scalar couplings in the arginine side chains of T4L L99A at 18.8 T and 278 K. The R14 side chain is flexible, while the R148 is rigid in agreement with relaxation measurements⁶. b Strips from a three-dimensional experiment to quantify long-range ¹³C^δ1–¹³C^α scalar couplings in isoleucine side chains of the 82-kDa MSG at 14.1 T and 310 K. The I238 side chain is dynamic around the χ₂ angle, as seen by the intermediate value of the ³J_CαCδ1 coupling constant, whereas I42 is more rigid in a trans conformation. Positive contours are depicted as red, while negative contours are in blue. Values for ³J_CαCδ1 in a and b are mean ± s.d.